5ACO

Cryo-EM structure of PGT128 Fab in complex with BG505 SOSIP.664 Env trimer

This is a non-PDB format compatible entry.

Summary for 5ACO

• Entry DOI: 10.2210/pdb5aco/pdb
• EMDB information: 3121
• Descriptor: HIV-1 ENVELOPE GLYCOPROTEIN, 2-acetamido-2-deoxy-beta-D-glucopyranose, PGT128 FAB, ... (10 entities in total)
• Functional Keywords: viral protein, immune system, hiv-1, env, bnab, antibody, pgt128
• Biological source: HUMAN IMMUNODEFICIENCY VIRUS 1; More
• Total number of polymer chains: 12
• Total formula weight: 391458.90

Authors

Lee, J.H.,Ward, A.B. (deposition date: 2015-08-17, release date: 2015-09-30, Last modification date: 2024-11-20)

Primary citation

Lee, J.H.,De Val, N.,Lyumkis, D.,Ward, A.B.
Model Building and Refinement of a Natively Glycosylated HIV-1 Env Protein by High-Resolution Cryoelectron Microscopy.
Structure, 23:1943-, 2015

PubMed Abstract: Secretory and membrane proteins from mammalian cells undergo post-translational modifications, including N-linked glycosylation, which can result in a large number of possible glycoforms. This sample heterogeneity can be problematic for structural studies, particularly X-ray crystallography. Thus, crystal structures of heavily glycosylated proteins such as the HIV-1 Env viral spike protein have been determined by removing the majority of glycans. This step is most frequently carried out using Endoglycosidase H (EndoH) and requires that all expressed glycans be in the high-mannose form, which is often not the native glycoform. With significantly improved technologies in single-particle cryoelectron microscopy, we demonstrate that it is now possible to refine and build natively glycosylated HIV-1 Env structures in solution to 4.36 Å resolution. At this resolution we can now analyze the complete epitope of a broadly neutralizing antibody (bnAb), PGT128, in the context of the trimer expressed with native glycans.

PubMed: 26388028
DOI: 10.1016/J.STR.2015.07.020

Experimental method

ELECTRON MICROSCOPY (4.36 Å)